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Kudin 2002 Mol Biol Rep - Revision history
2024-03-29T14:41:16Z
Revision history for this page on the wiki
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https://wiki.oroboros.at/index.php?title=Kudin_2002_Mol_Biol_Rep&diff=85788&oldid=prev
Bader Helga at 13:48, 24 March 2015
2015-03-24T13:48:29Z
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Mol Biol Rep</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Mol Biol Rep</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the <ins style="font-weight: bold; text-decoration: none;">''</ins>in vivo<ins style="font-weight: bold; text-decoration: none;">'' </ins>situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
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Bader Helga
https://wiki.oroboros.at/index.php?title=Kudin_2002_Mol_Biol_Rep&diff=81580&oldid=prev
Bader Helga at 13:25, 19 February 2015
2015-02-19T13:25:26Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 13:25, 19 February 2015</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|title=Kudin A, Vielhaber S, Elger CE, Kunz WS (2002) Differences in flux control and reserve capacity of cytochrome c oxidase (COX) in human skeletal muscle and brain suggest different metabolic effects of mild COX deficiencies. Mol Biol Rep 29: 89-92.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|title=Kudin A, Vielhaber S, Elger CE, Kunz WS (2002) Differences in flux control and reserve capacity of cytochrome c oxidase (COX) in human skeletal muscle and brain suggest different metabolic effects of mild COX deficiencies. Mol Biol Rep 29:89-92.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[http://www.ncbi.nlm.nih.gov/pubmed/12241082 PMID: 12241082]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[http://www.ncbi.nlm.nih.gov/pubmed/12241082 PMID: 12241082]</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">|instruments=Oxygraph-2k</del></div></td><td colspan="2"></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Human</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Human</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Skeletal muscle, Nervous system</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Skeletal muscle, Nervous system</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Homogenate</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Homogenate</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=Complex IV; <del style="font-weight: bold; text-decoration: none;">Cytochrome </del>c <del style="font-weight: bold; text-decoration: none;">Oxidase</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=Complex IV;<ins style="font-weight: bold; text-decoration: none;">cytochrome </ins>c <ins style="font-weight: bold; text-decoration: none;">oxidase</ins></div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
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Bader Helga
https://wiki.oroboros.at/index.php?title=Kudin_2002_Mol_Biol_Rep&diff=43163&oldid=prev
Meissner Barbara at 08:09, 27 February 2013
2013-02-27T08:09:14Z
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Skeletal muscle, <del style="font-weight: bold; text-decoration: none;">Neurons; Brain</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Skeletal muscle, <ins style="font-weight: bold; text-decoration: none;">Nervous system</ins></div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=Complex IV; Cytochrome c Oxidase</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=Complex IV; Cytochrome c Oxidase</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
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Meissner Barbara
https://wiki.oroboros.at/index.php?title=Kudin_2002_Mol_Biol_Rep&diff=30219&oldid=prev
Meissner Barbara at 14:05, 29 May 2012
2012-05-29T14:05:22Z
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2002</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2002</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|journal=<del style="font-weight: bold; text-decoration: none;">Molec </del>Biol Rep</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|journal=<ins style="font-weight: bold; text-decoration: none;">Mol </ins>Biol Rep</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
</table>
Meissner Barbara
https://wiki.oroboros.at/index.php?title=Kudin_2002_Mol_Biol_Rep&diff=27632&oldid=prev
Gnaiger Erich at 23:52, 4 April 2012
2012-04-04T23:52:35Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 23:52, 4 April 2012</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2002</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2002</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|journal=Molec<del style="font-weight: bold; text-decoration: none;">. </del>Biol<del style="font-weight: bold; text-decoration: none;">. </del>Rep<del style="font-weight: bold; text-decoration: none;">.</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|journal=Molec Biol Rep</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|instruments=Oxygraph-2k</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|instruments=Oxygraph-2k</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Human</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Human</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Skeletal <del style="font-weight: bold; text-decoration: none;">Muscle</del>, Neurons; Brain</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Skeletal <ins style="font-weight: bold; text-decoration: none;">muscle</ins>, Neurons; Brain</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized <del style="font-weight: bold; text-decoration: none;">Tissue</del>, Homogenate</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized <ins style="font-weight: bold; text-decoration: none;">tissue</ins>, Homogenate</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=Complex IV; Cytochrome c Oxidase</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=Complex IV; Cytochrome c Oxidase</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td></tr>
</table>
Gnaiger Erich
https://wiki.oroboros.at/index.php?title=Kudin_2002_Mol_Biol_Rep&diff=27016&oldid=prev
Eigentler Andrea at 11:53, 26 March 2012
2012-03-26T11:53:40Z
<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 11:53, 26 March 2012</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Skeletal Muscle, Neurons; Brain</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Skeletal Muscle, Neurons; Brain</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized <del style="font-weight: bold; text-decoration: none;">Cell or </del>Tissue<del style="font-weight: bold; text-decoration: none;">; </del>Homogenate</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized Tissue<ins style="font-weight: bold; text-decoration: none;">, </ins>Homogenate</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=Complex IV; Cytochrome c Oxidase</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=Complex IV; Cytochrome c Oxidase</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td></tr>
</table>
Eigentler Andrea
https://wiki.oroboros.at/index.php?title=Kudin_2002_Mol_Biol_Rep&diff=21192&oldid=prev
Harrison DK at 14:43, 13 December 2011
2011-12-13T14:43:20Z
<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:43, 13 December 2011</td>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|title=Kudin A, Vielhaber S, Elger CE, Kunz WS (2002) Differences in flux control and reserve capacity of cytochrome c oxidase (COX) in human skeletal muscle and brain suggest different metabolic effects of mild COX deficiencies. Mol<del style="font-weight: bold; text-decoration: none;">. </del>Biol<del style="font-weight: bold; text-decoration: none;">. </del>Rep<del style="font-weight: bold; text-decoration: none;">. </del>29: 89-92.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|title=Kudin A, Vielhaber S, Elger CE, Kunz WS (2002) Differences in flux control and reserve capacity of cytochrome c oxidase (COX) in human skeletal muscle and brain suggest different metabolic effects of mild COX deficiencies. Mol Biol Rep 29: 89-92.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[http://www.ncbi.nlm.nih.gov/pubmed/12241082 PMID: 12241082]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[http://www.ncbi.nlm.nih.gov/pubmed/12241082 PMID: 12241082]</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Kudin A, Vielhaber S, Elger CE, Kunz WS</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Kudin A, Vielhaber S, Elger CE, Kunz WS</div></td></tr>
</table>
Harrison DK
https://wiki.oroboros.at/index.php?title=Kudin_2002_Mol_Biol_Rep&diff=21190&oldid=prev
Harrison DK: moved Kudin 2002 MolBiolRep to Kudin 2002 Mol Biol Rep
2011-12-13T14:41:48Z
<p>moved <a href="/index.php/Kudin_2002_MolBiolRep" class="mw-redirect" title="Kudin 2002 MolBiolRep">Kudin 2002 MolBiolRep</a> to <a href="/index.php/Kudin_2002_Mol_Biol_Rep" title="Kudin 2002 Mol Biol Rep">Kudin 2002 Mol Biol Rep</a></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="1" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="1" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:41, 13 December 2011</td>
</tr><tr><td colspan="2" class="diff-notice" lang="en"><div class="mw-diff-empty">(No difference)</div>
</td></tr></table>
Harrison DK
https://wiki.oroboros.at/index.php?title=Kudin_2002_Mol_Biol_Rep&diff=15929&oldid=prev
Wiethuechter Anita at 09:09, 9 September 2011
2011-09-09T09:09:21Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 09:09, 9 September 2011</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Publication</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Publication</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|title=Kudin A, Vielhaber S, Elger CE, Kunz WS (2002) Differences in flux control and reserve capacity of cytochrome c oxidase (COX) in human skeletal muscle and brain suggest different metabolic effects of mild COX deficiencies. Mol. Biol. Rep. 29: 89-92.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|title=Kudin A, Vielhaber S, Elger CE, Kunz WS (2002) Differences in flux control and reserve capacity of cytochrome c oxidase (COX) in human skeletal muscle and brain suggest different metabolic effects of mild COX deficiencies. Mol. Biol. Rep. 29: 89-92.</div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">|info=[http://www.ncbi.nlm.nih.gov/pubmed/12241082 PMID: 12241082]</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Kudin A, Vielhaber S, Elger CE, Kunz WS</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Kudin A, Vielhaber S, Elger CE, Kunz WS</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2002</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2002</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Molec. Biol. Rep.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Molec. Biol. Rep.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue.</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|<del style="font-weight: bold; text-decoration: none;">info</del>=<del style="font-weight: bold; text-decoration: none;">[http://www.ncbi.nlm.nih.gov/pubmed/12241082 PMID: 12241082]</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|<ins style="font-weight: bold; text-decoration: none;">discipline</ins>=<ins style="font-weight: bold; text-decoration: none;">Mitochondrial Physiology</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Labeling</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Labeling</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|<del style="font-weight: bold; text-decoration: none;">discipline</del>=<del style="font-weight: bold; text-decoration: none;">Mitochondrial Physiology</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|<ins style="font-weight: bold; text-decoration: none;">instruments</ins>=<ins style="font-weight: bold; text-decoration: none;">Oxygraph-2k</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Human</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Human</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Skeletal Muscle, Neurons; Brain</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Skeletal Muscle, Neurons; Brain</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized Cell or Tissue; Homogenate</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized Cell or Tissue; Homogenate</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=<del style="font-weight: bold; text-decoration: none;">TCA Cycle and Matrix Dehydrogenases, Complex I, </del>Complex IV; Cytochrome c Oxidase</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=Complex IV; Cytochrome c Oxidase</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|<del style="font-weight: bold; text-decoration: none;">topics=Respiration; OXPHOS; ETS Capacity</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|<ins style="font-weight: bold; text-decoration: none;">discipline</ins>=<ins style="font-weight: bold; text-decoration: none;">Mitochondrial Physiology</ins></div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">|instruments</del>=<del style="font-weight: bold; text-decoration: none;">Oxygraph-2k</del></div></td><td colspan="2"></td></tr>
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Wiethuechter Anita
https://wiki.oroboros.at/index.php?title=Kudin_2002_Mol_Biol_Rep&diff=6629&oldid=prev
Biljana at 08:21, 20 October 2010
2010-10-20T08:21:53Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:21, 20 October 2010</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2002</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2002</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Molec. Biol. Rep.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Molec. Biol. Rep.</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue. </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[http://www.ncbi.nlm.nih.gov/pubmed/12241082 PMID: 12241082]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[http://www.ncbi.nlm.nih.gov/pubmed/12241082 PMID: 12241082]</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|instruments=Oxygraph-2k</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|instruments=Oxygraph-2k</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">|articletype=Protocol; Manual</del></div></td><td colspan="2"></td></tr>
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Biljana